Answer: Disrupting hydrogen bonds and hydrophobic interactions.
- A Hydrolytically cleaving the covalent peptide backbone of the protein
- B Disrupting hydrogen bonds and hydrophobic interactions
- C Chelating and stripping essential metal cofactors from the active site
- D Covalently adding phosphate groups onto serine and threonine residues
Correct answer: B. Disrupting hydrogen bonds and hydrophobic interactions
Explanation: Urea denatures proteins by forming hydrogen bonds with the backbone and disrupting internal H bonds and hydrophobic interactions that maintain tertiary structure. This unfolds the protein without cleaving peptide bonds.
As substrate concentration rises, reaction rate increases steeply at first, then plateaus at Vmax once every enzyme molecule is working at full capacity; Km is the substrate concentration giving half-maximal rate, and a LOWER Km means the enzyme reaches that rate with less substrate (higher affinity).
Concept context
Carbohydrates, proteins, lipids, nucleic acids, and enzyme kinetics. Essential foundation for understanding metabolism.